Determining Activation Energy from Rate Constant for an Enzyme-Catalyzed Reaction
Here is the problem I have to solve:
If 10 g of pure carbonic anhydrase catalyzes the hydration of 0.30 g of carbon dioxide in 1 min at 37 degrees C under optimal conditions, what is the turnover number (kcat) of carbonic anhydrase (in units of min-1)?
I have already calculated the turnover number, which is 2.0 x 107 min-1, but I'm kind of lost with two other questions.
(b) From the answer in (a) calculate the activation energy of the enzyme catalyzed reaction (in kJ/mol)
.
(c) If carbonic anhydrase provides a rate enhancement of 107, what is the activation energy for the uncatalyzed reaction?
https://brainmass.com/biology/enzyme-catalysts-and-reactions/determining-activation-energy-rate-constant-108800
Solution Preview
Please see attached file
From transition-state theory, an expression can be derived that relates the magnitude of a rate constant (k) to the activation energy:
k = (kT/h)e-G/RT
where k is the Boltzmann constant and h is Planck's constant. In this case, G is the activation energy ...
Solution Summary
This solution shows step-by-step calculations to determine the activation energy of the reaction with carbonic anhydrase and also the activation energy of the uncatalyzed reaction. Brief explanations are also included.